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Structure paper

TitleAsymmetric horseshoe-like assembly of peroxisomal yeast oxalyl-CoA synthetase.
Journal, issue, pagesBiol Chem, Vol. 404, Issue 2-3, Page 195-207, Year 2023
Publish dateJan 26, 2023
AuthorsJérôme Bürgi / Pascal Lill / Evdokia-Anastasia Giannopoulou / Cy M Jeffries / Grzegorz Chojnowski / Stefan Raunser / Christos Gatsogiannis / Matthias Wilmanns /
PubMed AbstractOxalyl-CoA synthetase from is one of the most abundant peroxisomal proteins in yeast and hence has become a model to study peroxisomal translocation. It contains a C-terminal Peroxisome Targeting ...Oxalyl-CoA synthetase from is one of the most abundant peroxisomal proteins in yeast and hence has become a model to study peroxisomal translocation. It contains a C-terminal Peroxisome Targeting Signal 1, which however is partly dispensable, suggesting additional receptor bindings sites. To unravel any additional features that may contribute to its capacity to be recognized as peroxisomal target, we determined its assembly and overall architecture by an integrated structural biology approach, including X-ray crystallography, single particle cryo-electron microscopy and small angle X-ray scattering. Surprisingly, it assembles into mixture of concentration-dependent dimers, tetramers and hexamers by dimer self-association. Hexameric particles form an unprecedented asymmetric horseshoe-like arrangement, which considerably differs from symmetric hexameric assembly found in many other protein structures. A single mutation within the self-association interface is sufficient to abolish any higher-level oligomerization, resulting in a homogenous dimeric assembly. The small C-terminal domain of yeast Oxalyl-CoA synthetase is connected by a partly flexible hinge with the large N-terminal domain, which provides the sole basis for oligomeric assembly. Our data provide a basis to mechanistically study peroxisomal translocation of this target.
External linksBiol Chem / PubMed:36694962
MethodsEM (single particle) / X-ray diffraction
Resolution2.45 - 3.1 Å
Structure data

15646

8atd

EMDB-15646, PDB-8atd:
Wild type hexamer oxalyl-CoA synthetase (OCS)
Method: EM (single particle) / Resolution: 3.1 Å

PDB-8aff:
Wild type oxalyl-CoA synthetase Pcs60p
Method: X-RAY DIFFRACTION / Resolution: 2.87 Å

PDB-8afg:
K352D oxalyl-CoA synthetase Pcs60p
Method: X-RAY DIFFRACTION / Resolution: 2.45 Å

Chemicals

ChemComp-HOH:
WATER / Water

ChemComp-SO4:
SULFATE ION / Sulfate

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsLIGASE / Peroxisome / Oxalyl-CoA ligase / Oligomer / Yeast

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